ArticleNeurochemical research1995
Characterization of squid enolase mRNA: sequence analysis, tissue distribution, and axonal localization.
Article in Neurochemical research, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 27 citations in OpenAlex.
- De novo assembly of a transcriptome from the eggs and early embryos of Astropecten aranciacus.PloS one · 2017Article
- Transcriptome analysis of embryonic and adult sensory axons reveals changes in mRNA repertoire localization.RNA (New York, N.Y.) · 2011Article
- The role of local protein synthesis and degradation in axon regeneration.Experimental neurology · 2010Review
- Cryptic peripheral ribosomal domains distributed intermittently along mammalian myelinated axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000Article
- Synthesis of beta-tubulin, actin, and other proteins in axons of sympathetic neurons in compartmented cultures.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- Active polysomes are present in the large presynaptic endings of the synaptosomal fraction from squid brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Enolase is a glycolytic enzyme whose amino acid sequence is highly conserved across a wide range of animal species. In mammals, enolase is known to be a dimeric protein composed of distinct but closely related subunits: alpha (non-neuronal), beta (muscle-specific), and gamma (neuron-specific). However, little information is available on the primary sequence of enolase in invertebrates. Here we report the isolation of two overlapping cDNA clones and the putative primary structure of the enzyme from the squid (Loligo pealii) nervous system. The composite sequence of those cDNA clones is 1575 bp and contains the entire coding region (1302 bp), as well as 66 and 207 bp of 5' and 3' untranslated sequence, respectively. Cross-species comparison of enolase primary structure reveals that squid enolase shares over 70% sequence identity to vertebrate forms of the enzyme. The greatest degree of sequence similarity was manifest to the alpha isoform of the human homologue. Results of Northern analysis revealed a single 1.6 kb mRNA species, the relative abundance of which differs approximately 10-fold between various tissues. Interestingly, evidence derived from in situ hybridization and polymerase chain reaction experiments indicate that the mRNA encoding enolase is present in the squid giant axon.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.